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2JB2

The structure of L-amino acid oxidase from Rhodococcus opacus in complex with L-phenylalanine.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001716molecular_functionL-amino-acid oxidase activity
A0005737cellular_componentcytoplasm
A0009063biological_processamino acid catabolic process
A0016491molecular_functionoxidoreductase activity
A0050025molecular_functionL-glutamate oxidase activity
A0050029molecular_functionL-lysine oxidase activity
A0106329molecular_functionL-phenylalaine oxidase activity
B0000166molecular_functionnucleotide binding
B0001716molecular_functionL-amino-acid oxidase activity
B0005737cellular_componentcytoplasm
B0009063biological_processamino acid catabolic process
B0016491molecular_functionoxidoreductase activity
B0050025molecular_functionL-glutamate oxidase activity
B0050029molecular_functionL-lysine oxidase activity
B0106329molecular_functionL-phenylalaine oxidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PHE A1490
ChainResidue
AARG84
AHOH2363
AGLN228
ATYR371
AALA466
ATRP467
AFAD1489
AHOH2062
AHOH2180
AHOH2354

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PHE B1490
ChainResidue
BARG84
BGLN228
BTYR371
BALA466
BTRP467
BFAD1489
BHOH2166
BHOH2336
BHOH2348

site_idAC3
Number of Residues35
DetailsBINDING SITE FOR RESIDUE FAD A1489
ChainResidue
AGLY19
AGLY21
APRO22
AALA23
AGLU42
AALA43
AARG44
AGLY49
AARG50
AGLY81
AALA82
ATHR83
AARG84
AALA259
AVAL261
ATHR292
ATYR371
ATRP416
ATYR421
AALA425
ATRP426
AGLY458
AASP459
AALA466
ATRP467
AGLN468
AALA471
APHE1490
AHOH2021
AHOH2066
AHOH2231
AHOH2325
AHOH2361
AHOH2362
AHOH2363

site_idAC4
Number of Residues37
DetailsBINDING SITE FOR RESIDUE FAD B1489
ChainResidue
BGLY19
BGLY21
BPRO22
BALA23
BLEU41
BGLU42
BALA43
BARG44
BGLY49
BARG50
BGLY81
BALA82
BTHR83
BARG84
BALA259
BVAL261
BTHR292
BILE293
BTYR371
BTRP416
BTYR421
BALA425
BTRP426
BGLY458
BASP459
BALA466
BTRP467
BGLN468
BALA471
BPHE1490
BHOH2022
BHOH2066
BHOH2210
BHOH2211
BHOH2346
BHOH2347
BHOH2348

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17234209","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2JAE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JB1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JB2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JB3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17234209","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2JB1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JB2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b5q
ChainResidueDetails
APRO86

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b5q
ChainResidueDetails
BPRO86

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b5q
ChainResidueDetails
ATYR78

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b5q
ChainResidueDetails
BTYR78

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PDB entries from 2025-10-08

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